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Protein

Beta-enolase

Gene

Eno3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to have a function in striated muscle development and regeneration.

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathway:iglycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase 2 (Pgk2)
  3. no protein annotated in this organism
  4. Enolase (Eno3), Enolase (Eno2), Enolase (Eno1), Enolase (Eno2), Enolase (Eno3), Enolase (Eno2), Enolase, Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3)
  5. Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Active sitei210 – 2101Proton donorBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi318 – 3181MagnesiumBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Active sitei343 – 3431Proton acceptorBy similarity
Binding sitei394 – 3941SubstrateBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.11. 3474.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name:
MSE
Skeletal muscle enolase
Gene namesi
Name:Eno3
Synonyms:Eno-3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95395. Eno3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 434433Beta-enolasePRO_0000134108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei44 – 441PhosphotyrosineBy similarity
Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
Modified residuei64 – 641N6-acetyllysineBy similarity
Modified residuei71 – 711N6-acetyllysineBy similarity
Modified residuei89 – 891N6-acetyllysine; alternateBy similarity
Modified residuei89 – 891N6-succinyllysine; alternateBy similarity
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei193 – 1931N6-acetyllysineBy similarity
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei202 – 2021N6-acetyllysineBy similarity
Modified residuei228 – 2281N6-acetyllysine; alternateBy similarity
Modified residuei228 – 2281N6-succinyllysine; alternateBy similarity
Modified residuei256 – 2561N6-acetyllysineBy similarity
Modified residuei263 – 2631PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei281 – 2811N6-acetyllysineBy similarity
Modified residuei287 – 2871PhosphotyrosineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei335 – 3351N6-acetyllysineBy similarity
Modified residuei343 – 3431N6-acetyllysineBy similarity
Modified residuei406 – 4061N6-acetyllysineBy similarity
Modified residuei420 – 4201N6-acetyllysine; alternateBy similarity
Modified residuei420 – 4201N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP21550.
PaxDbiP21550.
PRIDEiP21550.

2D gel databases

SWISS-2DPAGEP21550.
UCD-2DPAGEP21550.

PTM databases

PhosphoSiteiP21550.

Expressioni

Tissue specificityi

The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I.1 Publication

Developmental stagei

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube.2 Publications

Inductioni

Levels decrease in degenerating myofibers, and increase with their regeneration.

Gene expression databases

BgeeiP21550.
CleanExiMM_ENO3.
ExpressionAtlasiP21550. baseline and differential.
GenevisibleiP21550. MM.

Interactioni

Subunit structurei

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD (By similarity).By similarity

Protein-protein interaction databases

BioGridi199453. 3 interactions.
IntActiP21550. 4 interactions.
MINTiMINT-1855839.
STRINGi10090.ENSMUSP00000072620.

Structurei

3D structure databases

ProteinModelPortaliP21550.
SMRiP21550. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP21550.
KOiK01689.
OMAiFRHPKIN.
PhylomeDBiP21550.
TreeFamiTF300391.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKARYLGK GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLVLPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE
260 270 280 290 300
FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD
310 320 330 340 350
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV
360 370 380 390 400
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEALGDK AVFAGRKFRN PKAK
Length:434
Mass (Da):47,025
Last modified:January 23, 2007 - v3
Checksum:iA1F757D83709D2B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2352AG → NA in AAA37554 (PubMed:2734297).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61600 Genomic DNA. Translation: CAA43797.1.
X57747 mRNA. Translation: CAA40913.1.
X62667 mRNA. Translation: CAA44540.1.
AK002485 mRNA. Translation: BAB22137.1.
BC013460 mRNA. Translation: AAH13460.1.
M20745 mRNA. Translation: AAA37554.1.
CCDSiCCDS24961.1.
PIRiS17109. NOMSB.
RefSeqiNP_001129534.1. NM_001136062.2.
NP_001263214.1. NM_001276285.1.
NP_031959.1. NM_007933.3.
XP_006532225.1. XM_006532162.2.
XP_006537193.1. XM_006537130.2.
UniGeneiMm.251322.
Mm.491763.

Genome annotation databases

EnsembliENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
GeneIDi13808.
KEGGimmu:13808.
UCSCiuc007jvx.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61600 Genomic DNA. Translation: CAA43797.1.
X57747 mRNA. Translation: CAA40913.1.
X62667 mRNA. Translation: CAA44540.1.
AK002485 mRNA. Translation: BAB22137.1.
BC013460 mRNA. Translation: AAH13460.1.
M20745 mRNA. Translation: AAA37554.1.
CCDSiCCDS24961.1.
PIRiS17109. NOMSB.
RefSeqiNP_001129534.1. NM_001136062.2.
NP_001263214.1. NM_001276285.1.
NP_031959.1. NM_007933.3.
XP_006532225.1. XM_006532162.2.
XP_006537193.1. XM_006537130.2.
UniGeneiMm.251322.
Mm.491763.

3D structure databases

ProteinModelPortaliP21550.
SMRiP21550. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199453. 3 interactions.
IntActiP21550. 4 interactions.
MINTiMINT-1855839.
STRINGi10090.ENSMUSP00000072620.

PTM databases

PhosphoSiteiP21550.

2D gel databases

SWISS-2DPAGEP21550.
UCD-2DPAGEP21550.

Proteomic databases

MaxQBiP21550.
PaxDbiP21550.
PRIDEiP21550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
GeneIDi13808.
KEGGimmu:13808.
UCSCiuc007jvx.3. mouse.

Organism-specific databases

CTDi2027.
MGIiMGI:95395. Eno3.

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP21550.
KOiK01689.
OMAiFRHPKIN.
PhylomeDBiP21550.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BRENDAi4.2.1.11. 3474.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.

Miscellaneous databases

NextBioi284592.
PROiP21550.
SOURCEiSearch...

Gene expression databases

BgeeiP21550.
CleanExiMM_ENO3.
ExpressionAtlasiP21550. baseline and differential.
GenevisibleiP21550. MM.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Lamande N., Brosset S., Keller A., Lucas M., Lazar M.
    Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: BALB/c and Swiss Webster.
    Tissue: Liver and Skeletal muscle.
  2. "Beta-enolase is a marker of human myoblast heterogeneity prior to differentiation."
    Peterson C.A., Cho M., Rastinejad F., Blau H.M.
    Dev. Biol. 151:626-629(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  5. Lubec G., Kang S.U., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression."
    Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F., Legault-Demare L., Lazar M.
    Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
  7. "Activation of the gene encoding the glycolytic enzyme beta-enolase during early myogenesis precedes an increased expression during fetal muscle development."
    Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M., Lazar M.
    Mech. Dev. 38:41-54(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION DURING MYOGENESIS.
  8. "Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."
    Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.
    Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  9. "Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
    Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
    Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
  10. "Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
    Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
    Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Differential modulation of alpha, beta and gamma enolase isoforms in regenerating mouse skeletal muscle."
    Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H., Keller A.
    Eur. J. Biochem. 267:3735-3743(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION REGULATION.

Entry informationi

Entry nameiENOB_MOUSE
AccessioniPrimary (citable) accession number: P21550
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.